Literature summary for 3.4.25.2 extracted from

Dong, S.; Hu, W.; Ge, Y.; Ojcius, D.; Lin, X.; Yan, J.
A leptospiral AAA+ chaperone-Ntn peptidase complex, HslUV, contributes to the intracellular survival of Leptospira interrogans in hosts and the transmission of leptospirosis (2017), Emerg. Microbes Infect., 6, e105 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Leptospira interrogans serovar Canicola	A0A0N7ELI3 and A0A0N9ELN0	A0A0N7ELI3 i.e. subunit HslV, A0A0N9ELN0 i.e. subunit HslU	-

Synonyms

Synonyms	Comment	Organism
HslUV	-	Leptospira interrogans serovar Canicola

General Information

General Information	Comment	Organism
physiological function	leptospiral HslUV is an ATP-dependent chaperone-peptidase complex containing ATPase associated with various cellular activity (AAA+) and N-terminal nucleophile (Ntn) hydrolase superfamily domains, respectively, which hydrolyzes casein and chymotrypsin-like substrates. Hydrolysis is blocked by threonine protease inhibitors. The infection of J774A.1 acrophages causes the increase of leptospiral denatured protein aggresomes, but more aggresomes accumulate in hslUV gene-deleted mutant. Compared to the wild-type strain, infection of cells in vitro with the mutant result in a higher number of dead leptospires, less leptospiral colonyforming units and lower growth ability, but also display a lower half lethal dose, attenuated histopathological injury and decreased leptospiral loading in lungs, liver, kidneys, peripheral blood and urine in hamsters	Leptospira interrogans serovar Canicola

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Release 2023.1 (January 2023)